Detection of protease inhibitory activity using X-ray film. Trypsin (5, 10 & 15%, w/v in Tris-HCl buffer) cleared the gelatin coat on film (Figure 1A-ii, iii & iv). Buffer alone served as control (Fig. 1 A-i). Trypsin (10%), preincubated with heat-treated crude seed extract (2 μg ml-1) for 60 min., was moderately inhibited and partial gelatin clearance was observed (Figure 1 B-ii). At higher concentrations (5, 12.5 μg ml-1), trypsin was completely inhibited and no gelatin digestion was seen (Figure 1 B-iii, iv). The heat-treated plant material (no endoproteolytic activity) served as control (Fig1 B-i). The inhibitory effect against Aspegillus flavus and Bacillus sp. protease is shown in Figure 1 C & D respectively. Aspegillus flavus and Bacillus sp. protease caused gelatin digestion (Figure 1 C-ii & D-ii) which upon incubation with seed extract was not seen (Figure 1 C-iii, iv & D-iii, iv). Buffer alone (Figure 1C -i), heat treated (Figure 1D -i) and inactivated seed extract (Figure 1C -v & D -v) served as control.